Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates
| Autor: | Fernando Moro, Judit Perales-Calvo, Arturo Muga |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
endocrine system
Protein Folding Chaperonins Proteolysis Protein domain Plasma protein binding Biology Biochemistry Mass Spectrometry Chaperonin Protein–protein interaction Substrate Specificity Protein structure medicine Escherichia coli Trypsin Cloning Molecular Molecular Biology medicine.diagnostic_test Escherichia coli Proteins Substrate (chemistry) Cell Biology HSP40 Heat-Shock Proteins Protein Structure Tertiary Cross-Linking Reagents Mutation Protein Structure and Folding Biophysics Anisotropy Protein folding Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | The Journal of biological chemistry. 285(44) |
| ISSN: | 1083-351X |
| Popis: | DnaJ from Escherichia coli is a Type I Hsp40 that functions as a cochaperone of DnaK (Hsp70), stimulating its ATPase activity and delivering protein substrates. How DnaJ binds protein substrates is still poorly understood. Here we have studied the role of DnaJ G/F-rich domain in binding of several substrates with different conformational properties (folded, partially (un)folded and unfolded). Using partial proteolysis we find that RepE, a folded substrate, contacts a wide DnaJ area that involves part of the G/F-rich region and Zn-binding domain. Deletion of G/F-rich region hampers binding of native RepE and reduced the affinity for partially (un)folded substrates. However, binding of completely unfolded substrates is independent on the G/F-rich region. These data indicate that DnaJ distinguishes the substrate conformation and is able to adapt the use of the G/F-rich region to form stable substrate complexes. |
| Databáze: | OpenAIRE |
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